Thermal Stabilization of Proteins by Mono- and Oligosaccharides: Measurement and Analysis in the Context of an Excluded Volume Model
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- 作者：Ilyas Beg ; Allen P. Minton ; Md. Imtaiyaz Hassan ; Asimul Islam ; Faizan Ahmad
- 刊名：Biochemistry
- 出版年：2015
- 出版时间：June 16, 2015
- 年：2015
- 卷：54
- 期：23
- 页码：3594-3603
- 全文大小：494K
- ISSN：1520-4995
文摘
The reversible thermal denaturation of apo 伪-lactalbumin and lysozyme was monitored via measurement of changes in absorbance and ellipticity in the presence of varying concentrations of seven mono- and oligosaccharides: glucose, galactose, fructose, sucrose, trehalose, raffinose, and stachyose. The temperature dependence of the unfolding curves was quantitatively accounted for by a two-state model, according to which the free energy of unfolding is increased by an amount that is independent of temperature and depends linearly upon the concentration of added saccharide. The increment of added unfolding free energy per mole of added saccharide was found to depend approximately linearly upon the extent of oligomerization of the saccharide. The relative strength of stabilization of different saccharide oligomers could be accounted for by a simplified statistical鈥搕hermodynamic model attributing the stabilization effect to volume exclusion deriving from steric repulsion between protein and saccharide molecules.